Shining light on cysteine modification: connecting protein conformational dynamics to catalysis and regulation.

ABSTRACT: Cysteine is a rare but functionally important amino acid that is often subject to covalent modification. Cysteine oxidation plays an important role in many human disease processes, and basal levels of cysteine oxidation are required for proper cellular function. Because reactive cysteine residues are typically ionized to the thiolate anion (Cys-S^-), their formation of a covalent bond alters the electrostatic and steric environment of the active site. X-ray-induced photo-oxidation to sulfenic acids (Cys-SOH) can recapitulate some aspects of the changes that occur under physiological conditions. Here we propose how site-specific cysteine photo-oxidation can be used to interrogate ensuing changes in protein structure and dynamics at atomic resolution. Although this powerful approac

SUBMITTER: van den Bedem H 

PROVIDER: S-EPMC6613112 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature